Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 16, Issue 1, Pages 1293-1311Publisher
MDPI
DOI: 10.3390/ijms16011293
Keywords
bifunctional enzyme-active alcohol dehydrogenase (ADHa); ethanol-acetaldehyde-oxidation; Gluconacetobacter diazotrophicus; acetic acid bacteria; alcohol aldehyde dehydrogenase
Funding
- CONACYT
- Saul Gomez-Manzo [154570]
- Gabriel Lopez-Velazquez [J43022-M, 62321]
- J43022-M and 62321)
- America Vanoye-Carlo [157863]
- Martha Elena Sosa-Torres [128921]
- CONACyT [2184, 2057]
- INP [089/2012]
- DGAPA-UNAM [IN231111]
- University of Konstanz [Kr 04/75]
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Gluconacetobacter diazotrophicus is a N-2-fixing bacterium endophyte from sugar cane. The oxidation of ethanol to acetic acid of this organism takes place in the periplasmic space, and this reaction is catalyzed by two membrane-bound enzymes complexes: the alcohol dehydrogenase (ADH) and the aldehyde dehydrogenase (ALDH). We present strong evidence showing that the well-known membrane-bound Alcohol dehydrogenase (ADHa) of Ga. diazotrophicus is indeed a double function enzyme, which is able to use primary alcohols (C2-C6) and its respective aldehydes as alternate substrates. Moreover, the enzyme utilizes ethanol as a substrate in a reaction mechanism where this is subjected to a two-step oxidation process to produce acetic acid without releasing the acetaldehyde intermediary to the media. Moreover, we propose a mechanism that, under physiological conditions, might permit a massive conversion of ethanol to acetic acid, as usually occurs in the acetic acid bacteria, but without the transient accumulation of the highly toxic acetaldehyde.
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